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分泌蛋白的新途径?

A novel pathway for secretory proteins?

作者信息

Muesch A, Hartmann E, Rohde K, Rubartelli A, Sitia R, Rapoport T A

机构信息

Zentralinstitut fuer Molekularbiologie der AdW der DDR, Berlin-Buch.

出版信息

Trends Biochem Sci. 1990 Mar;15(3):86-8. doi: 10.1016/0968-0004(90)90186-f.

Abstract

In eukaryotes, most proteins which are transported to the extracellular space, into mitochondria or into chloroplasts are synthesized as precursor polypeptides containing cleavable N-terminal signal or targeting sequences. We have searched the literature for proteins that are exported from the cytosol without being proteolytically processed. Some of these proteins contain uncleaved signal or targeting sequences. However, among secretory proteins there is a class that does not possess hydrophobic signal sequences and appears to leave the cell by a secretory pathway clearly distinct from the classical route through the endoplasmic reticulum and Golgi apparatus.

摘要

在真核生物中,大多数被转运到细胞外空间、线粒体或叶绿体中的蛋白质都是以前体多肽的形式合成的,这些前体多肽含有可裂解的N端信号或靶向序列。我们在文献中搜索了那些未经蛋白水解加工就从细胞质中输出的蛋白质。其中一些蛋白质含有未切割的信号或靶向序列。然而,在分泌蛋白中,有一类蛋白质不具有疏水信号序列,似乎是通过一条明显不同于通过内质网和高尔基体的经典途径的分泌途径离开细胞的。

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